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P20333

- TNR1B_HUMAN

UniProt

P20333 - TNR1B_HUMAN

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Protein

Tumor necrosis factor receptor superfamily member 1B

Gene
TNFRSF1B, TNFBR, TNFR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. tumor necrosis factor-activated receptor activity Source: ProtInc
  3. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular response to growth factor stimulus Source: Ensembl
  3. cellular response to lipopolysaccharide Source: BHF-UCL
  4. immune response Source: Ensembl
  5. inflammatory response Source: Ensembl
  6. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  7. negative regulation of inflammatory response Source: Ensembl
  8. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  9. RNA destabilization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 1B
Alternative name(s):
Tumor necrosis factor receptor 2
Short name:
TNF-R2
Tumor necrosis factor receptor type II
Short name:
TNF-RII
Short name:
TNFR-II
p75
p80 TNF-alpha receptor
CD_antigen: CD120b
INN: Etanercept
Cleaved into the following 2 chains:
Gene namesi
Synonyms:TNFBR, TNFR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:11917. TNFRSF1B.

Subcellular locationi

Isoform 1 : Cell membrane; Single-pass type I membrane protein 1 Publication
Isoform 2 : Secreted 1 Publication
Chain Tumor necrosis factor-binding protein 2 : Secreted 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 257235Extracellular Reviewed predictionAdd
BLAST
Transmembranei258 – 28730Helical; Reviewed predictionAdd
BLAST
Topological domaini288 – 461174Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane raft Source: BHF-UCL
  4. neuronal cell body Source: Ensembl
  5. nucleus Source: Ensembl
  6. perinuclear region of cytoplasm Source: Ensembl
  7. plasma membrane Source: UniProtKB-SubCell
  8. varicosity Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Pharmaceutical usei

Available under the name Enbrel (Immunex and Wyeth-Ayerst). Used to treat moderate to severe rheumatoid arthritis (RA). Enbrel consist of the extracellular ligand-binding portion of TNFRSF1B linked to an immunoglobulin Fc chain. It binds to TNF-alpha and blocks its interactions with receptors.

Organism-specific databases

PharmGKBiPA36610.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 461439Tumor necrosis factor receptor superfamily member 1b, membrane formPRO_0000034548Add
BLAST
Chaini27 – ?Tumor necrosis factor-binding protein 2PRO_0000034549

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 53 By similarity
Disulfide bondi54 ↔ 67 By similarity
Disulfide bondi57 ↔ 75 By similarity
Disulfide bondi78 ↔ 93 By similarity
Disulfide bondi96 ↔ 110 By similarity
Disulfide bondi100 ↔ 118 By similarity
Disulfide bondi120 ↔ 126 By similarity
Disulfide bondi134 ↔ 143 By similarity
Disulfide bondi137 ↔ 161 By similarity
Disulfide bondi164 ↔ 179 By similarity
Glycosylationi171 – 1711N-linked (GlcNAc...) Reviewed prediction
Glycosylationi193 – 1931N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Phosphorylated; mainly on serine residues and with a very low level on threonine residues.
A soluble form (tumor necrosis factor binding protein 2) is produced from the membrane form by proteolytic processing.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP20333.
PeptideAtlasiP20333.
PRIDEiP20333.

PTM databases

PhosphoSiteiP20333.

Miscellaneous databases

PMAP-CutDBP20333.

Expressioni

Gene expression databases

ArrayExpressiP20333.
BgeeiP20333.
CleanExiHS_TNFRSF1B.
GenevestigatoriP20333.

Organism-specific databases

HPAiCAB013045.
HPA004796.

Interactioni

Subunit structurei

Binds to TRAF2. Interacts with BMX.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRNP287995EBI-358983,EBI-747754
TNFP013752EBI-358983,EBI-359977
TRAF2Q129333EBI-358983,EBI-355744

Protein-protein interaction databases

BioGridi112987. 26 interactions.
DIPiDIP-78N.
IntActiP20333. 12 interactions.
MINTiMINT-134958.
STRINGi9606.ENSP00000365435.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 474
Turni48 – 514
Beta strandi52 – 554
Beta strandi61 – 655
Beta strandi74 – 774
Beta strandi86 – 883
Beta strandi104 – 1085
Beta strandi112 – 1143
Beta strandi117 – 1204
Beta strandi124 – 1296
Beta strandi131 – 1399
Beta strandi147 – 1515
Turni154 – 1563
Beta strandi160 – 1634
Beta strandi174 – 1763
Beta strandi194 – 1963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CA9X-ray2.30G/H420-428[»]
3ALQX-ray3.00R/S/T/U/V/W33-205[»]
ProteinModelPortaliP20333.
SMRiP20333. Positions 37-200.

Miscellaneous databases

EvolutionaryTraceiP20333.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati39 – 7638TNFR-Cys 1Add
BLAST
Repeati77 – 11842TNFR-Cys 2Add
BLAST
Repeati119 – 16244TNFR-Cys 3Add
BLAST
Repeati163 – 20139TNFR-Cys 4Add
BLAST

Sequence similaritiesi

Contains 4 TNFR-Cys repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42764.
HOGENOMiHOG000132845.
HOVERGENiHBG054237.
InParanoidiP20333.
KOiK05141.
OMAiGNASMDA.
OrthoDBiEOG786H2Q.
PhylomeDBiP20333.
TreeFamiTF331157.

Family and domain databases

InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020411. TNFR_1B.
[Graphical view]
PfamiPF00020. TNFR_c6. 2 hits.
[Graphical view]
PRINTSiPR01919. TNFACTORR1B.
SMARTiSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEiPS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20333-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA    50
QMCCSKCSPG QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC 100
SSDQVETQAC TREQNRICTC RPGWYCALSK QEGCRLCAPL RKCRPGFGVA 150
RPGTETSDVV CKPCAPGTFS NTTSSTDICR PHQICNVVAI PGNASMDAVC 200
TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS FLLPMGPSPP 250
AEGSTGDFAL PVGLIVGVTA LGLLIIGVVN CVIMTQVKKK PLCLQREAKV 300
PHLPADKARG TQGPEQQHLL ITAPSSSSSS LESSASALDR RAPTRNQPQA 350
PGVEASGAGE ARASTGSSDS SPGGHGTQVN VTCIVNVCSS SDHSSQCSSQ 400
ASSTMGDTDS SPSESPKDEQ VPFSKEECAF RSQLETPETL LGSTEEKPLP 450
LGVPDAGMKP S 461
Length:461
Mass (Da):48,291
Last modified:May 27, 2002 - v3
Checksum:i603D0AE1CD69ACBF
GO
Isoform 2 (identifier: P20333-2) [UniParc]FASTAAdd to Basket

Also known as: DS-TNFR2(Delta7,8), sTNFR2

The sequence of this isoform differs from the canonical sequence as follows:
     263-268: GLIVGV → ASLACR
     269-461: Missing.

Show »
Length:268
Mass (Da):28,461
Checksum:i51A97BA5222FA444
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871V → M.1 Publication
Corresponds to variant rs2228494 [ dbSNP | Ensembl ].
VAR_017176
Natural varianti196 – 1961M → R Frequent polymorphism; seems to be associated with hyperandrogenism, polycystic ovary syndrome (PCOS) and systemic lupus erythematosus. 7 Publications
Corresponds to variant rs1061622 [ dbSNP | Ensembl ].
VAR_015434
Natural varianti232 – 2321E → K.4 Publications
Corresponds to variant rs5746026 [ dbSNP | Ensembl ].
VAR_015435
Natural varianti236 – 2361A → T.1 Publication
Corresponds to variant rs5746027 [ dbSNP | Ensembl ].
VAR_017177
Natural varianti264 – 2641L → P.1 Publication
Corresponds to variant rs2229700 [ dbSNP | Ensembl ].
VAR_017178
Natural varianti269 – 2691T → P.1 Publication
Corresponds to variant rs17879042 [ dbSNP | Ensembl ].
VAR_017179
Natural varianti295 – 2951Q → R.1 Publication
Corresponds to variant rs5746032 [ dbSNP | Ensembl ].
VAR_017180
Natural varianti301 – 3011P → R.1 Publication
Corresponds to variant rs17883432 [ dbSNP | Ensembl ].
VAR_017181

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei263 – 2686GLIVGV → ASLACR in isoform 2. VSP_011826
Alternative sequencei269 – 461193Missing in isoform 2. VSP_011827Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 373EPG → APT AA sequence 1 Publication
Sequence conflicti98 – 981S → P in AAN72434. 1 Publication
Sequence conflicti102 – 1021S → P in AAN72434. 1 Publication
Sequence conflicti141 – 1411R → P in AAA63262. 1 Publication
Sequence conflicti363 – 3631A → T in AAA63262. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55994 mRNA. Translation: AAA36755.1.
M32315 mRNA. Translation: AAA59929.1.
U52165
, U52156, U52157, U52158, U52159, U52160, U52161, U52162, U52163, U52164 Genomic DNA. Translation: AAC50622.1.
AY148473 mRNA. Translation: AAN72434.1.
BT019927 mRNA. Translation: AAV38730.1.
AY264804 Genomic DNA. Translation: AAO89076.1.
AY342040 Genomic DNA. Translation: AAP88939.1.
AL031276, AL357835 Genomic DNA. Translation: CAI19225.1.
AL357835, AL031276 Genomic DNA. Translation: CAH73721.1.
CH471130 Genomic DNA. Translation: EAW71733.1.
BC052977 mRNA. Translation: AAH52977.1.
S63368 mRNA. Translation: AAB19824.2.
M35857 mRNA. Translation: AAA63262.1.
AB030950 Genomic DNA. Translation: BAA89053.1.
CCDSiCCDS145.1. [P20333-1]
PIRiA35356.
RefSeqiNP_001057.1. NM_001066.2. [P20333-1]
UniGeneiHs.256278.

Genome annotation databases

EnsembliENST00000376259; ENSP00000365435; ENSG00000028137. [P20333-1]
GeneIDi7133.
KEGGihsa:7133.
UCSCiuc001att.3. human. [P20333-1]

Polymorphism databases

DMDMi21264534.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
NIEHS-SNPs
Enbrel

Clinical information on Enbrel

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55994 mRNA. Translation: AAA36755.1 .
M32315 mRNA. Translation: AAA59929.1 .
U52165
, U52156 , U52157 , U52158 , U52159 , U52160 , U52161 , U52162 , U52163 , U52164 Genomic DNA. Translation: AAC50622.1 .
AY148473 mRNA. Translation: AAN72434.1 .
BT019927 mRNA. Translation: AAV38730.1 .
AY264804 Genomic DNA. Translation: AAO89076.1 .
AY342040 Genomic DNA. Translation: AAP88939.1 .
AL031276 , AL357835 Genomic DNA. Translation: CAI19225.1 .
AL357835 , AL031276 Genomic DNA. Translation: CAH73721.1 .
CH471130 Genomic DNA. Translation: EAW71733.1 .
BC052977 mRNA. Translation: AAH52977.1 .
S63368 mRNA. Translation: AAB19824.2 .
M35857 mRNA. Translation: AAA63262.1 .
AB030950 Genomic DNA. Translation: BAA89053.1 .
CCDSi CCDS145.1. [P20333-1 ]
PIRi A35356.
RefSeqi NP_001057.1. NM_001066.2. [P20333-1 ]
UniGenei Hs.256278.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CA9 X-ray 2.30 G/H 420-428 [» ]
3ALQ X-ray 3.00 R/S/T/U/V/W 33-205 [» ]
ProteinModelPortali P20333.
SMRi P20333. Positions 37-200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112987. 26 interactions.
DIPi DIP-78N.
IntActi P20333. 12 interactions.
MINTi MINT-134958.
STRINGi 9606.ENSP00000365435.

Chemistry

ChEMBLi CHEMBL1250356.
DrugBanki DB00005. Etanercept.
DB00065. Infliximab.
GuidetoPHARMACOLOGYi 1871.

PTM databases

PhosphoSitei P20333.

Polymorphism databases

DMDMi 21264534.

Proteomic databases

PaxDbi P20333.
PeptideAtlasi P20333.
PRIDEi P20333.

Protocols and materials databases

DNASUi 7133.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376259 ; ENSP00000365435 ; ENSG00000028137 . [P20333-1 ]
GeneIDi 7133.
KEGGi hsa:7133.
UCSCi uc001att.3. human. [P20333-1 ]

Organism-specific databases

CTDi 7133.
GeneCardsi GC01P012161.
HGNCi HGNC:11917. TNFRSF1B.
HPAi CAB013045.
HPA004796.
MIMi 191191. gene.
neXtProti NX_P20333.
PharmGKBi PA36610.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42764.
HOGENOMi HOG000132845.
HOVERGENi HBG054237.
InParanoidi P20333.
KOi K05141.
OMAi GNASMDA.
OrthoDBi EOG786H2Q.
PhylomeDBi P20333.
TreeFami TF331157.

Miscellaneous databases

EvolutionaryTracei P20333.
GeneWikii TNFRSF1B.
GenomeRNAii 7133.
NextBioi 27909.
PMAP-CutDB P20333.
PROi P20333.
SOURCEi Search...

Gene expression databases

ArrayExpressi P20333.
Bgeei P20333.
CleanExi HS_TNFRSF1B.
Genevestigatori P20333.

Family and domain databases

InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020411. TNFR_1B.
[Graphical view ]
Pfami PF00020. TNFR_c6. 2 hits.
[Graphical view ]
PRINTSi PR01919. TNFACTORR1B.
SMARTi SM00208. TNFR. 4 hits.
[Graphical view ]
PROSITEi PS00652. TNFR_NGFR_1. 2 hits.
PS50050. TNFR_NGFR_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor."
    Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W., Hale K.K., Squires C.H., Thompson R.C., Vannice J.L.
    Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-196.
  2. "A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins."
    Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R., Dower S.K., Cosman D., Goodwin R.G.
    Science 248:1019-1023(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  4. "Identification and characterization of a novel spliced variant that encodes human soluble tumor necrosis factor receptor 2."
    Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D., Ricart W., Engel P.
    Int. Immunol. 16:169-177(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION (ISOFORM 2).
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. NIEHS SNPs program
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-187; ARG-196; LYS-232; THR-236; PRO-264 AND ARG-295.
  7. SeattleSNPs variation discovery resource
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-196; LYS-232; PRO-269 AND ARG-301.
  8. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: PNS.
  11. "Purification and partial amino acid sequence analysis of two distinct tumor necrosis factor receptors from HL60 cells."
    Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W., Brockhaus M.
    J. Biol. Chem. 265:20131-20138(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
  12. "Purification of two types of TNF inhibitors in the urine of the patient with chronic glomerulonephritis."
    Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.
    Nephron 66:386-390(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-37.
    Tissue: Urine.
  13. "Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors."
    Engelmann H., Novick D., Wallach D.
    J. Biol. Chem. 265:1531-1536(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-31.
    Tissue: Urine.
  14. "Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences."
    Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R., Brockhaus M., Lesslauer W.
    Cytokine 2:231-237(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
  15. "Complementary DNA cloning of a receptor for tumor necrosis factor and demonstration of a shed form of the receptor."
    Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D., Ringold G.M.
    Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT ARG-196.
  16. "New single nucleotide polymorphisms in the coding region of human TNFR2: association with systemic lupus erythematosus."
    Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K.
    Genes Immun. 1:501-503(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, VARIANTS ARG-196 AND LYS-232.
  17. "Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation."
    Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M., Lipari M.T., Goeddel D.V.
    J. Biol. Chem. 267:21172-21178(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  18. "A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor."
    Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.
    Cell 78:681-692(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2.
  19. "Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role in endothelial cell migration and angiogenesis."
    Pan S., An P., Zhang R., He X., Yin G., Min W.
    Mol. Cell. Biol. 22:7512-7523(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BMX.
  20. "Structural basis for self-association and receptor recognition of human TRAF2."
    Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.
    Nature 398:533-538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH TRAF2.
  21. "Association of tumor necrosis factor receptor type II polymorphism 196R with systemic lupus erythematosus in the Japanese: molecular and functional analysis."
    Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y., Arinobu Y., Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y.
    Arthritis Rheum. 44:2819-2827(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-196 AND LYS-232.
  22. "Comment: the methionine 196 arginine polymorphism in exon 6 of the TNF receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary syndrome and hyperandrogenism."
    Peral B., San Millan J.L., Castello R., Moghetti P., Escobar-Morreale H.F.
    J. Clin. Endocrinol. Metab. 87:3977-3983(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-196.

Entry informationi

Entry nameiTNR1B_HUMAN
AccessioniPrimary (citable) accession number: P20333
Secondary accession number(s): B1AJZ3
, Q16042, Q6YI29, Q9UIH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 27, 2002
Last modified: September 3, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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